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Taipale_HSP90_cochaperone_P77_VS5

ABSTRACT: This submission is part of the mass spectrometry datasets for the manuscript by Taipale et al. (HSP90 cochaperone interaction network); Cell, 2014. This submission contains files for the data presented as a supplementary figure that details differences in interaction profiles obtained by tagging proteins either at the amino- or carboxy-termini, all acquired on a 5600 TripleTOF mass spectrometer. See the README file within "Methods and Protocols" and the accompanying File description.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Anne-Claude Gingras

PROVIDER: MSV000078574 | MassIVE | Wed Apr 02 16:23:00 BST 2014

REPOSITORIES: MassIVE

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Publications

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

Taipale Mikko M Tucker George G Peng Jian J Krykbaeva Irina I Lin Zhen-Yuan ZY Larsen Brett B Choi Hyungwon H Berger Bonnie B Gingras Anne-Claude AC Lindquist Susan S

Cell 20140701 2

Chaperones are abundant cellular proteins that promote the folding and function of their substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set of cofactors (cochaperones) that regulate their specificity and function. However, how these cochaperones regulate protein folding and whether they have chaperone-independent biological functions is largely unknown. We combined mass spectrometry and quantitative high-throughput LUMIER assays to systematically charac ...[more]

PMID: 25036637

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